EzCatDB: T00008

DB codeT00008
CATH domainDomain 11.10.540.10
Domain 22.40.110.10
Domain 31.20.140.10Catalytic domain
E.C.1.3.8.7
CSA3mdd

CATH domainRelated DB codes (homologues)
1.10.540.10T00007,T00009
1.20.140.10T00007,T00009
2.40.110.10T00007,T00009

Enzyme Name
Swiss-protKEGG

Q72JJ3Q5SGZ2P41367P11310
Protein name

Medium-chain specific acyl-CoA dehydrogenase, mitochondrialMedium-chain specific acyl-CoA dehydrogenase, mitochondrialmedium-chain acyl-CoA dehydrogenase
fatty acyl coenzyme A dehydrogenase (ambiguous)
acyl coenzyme A dehydrogenase (ambiguous)
acyl dehydrogenase (ambiguous)
fatty-acyl-CoA dehydrogenase (ambiguous)
acyl CoA dehydrogenase (ambiguous)
general acyl CoA dehydrogenase (ambiguous)
medium-chain acyl-coenzyme A dehydrogenase
acyl-CoA:(acceptor) 2,3-oxidoreductase (ambiguous)
ACADM (gene name)
SynonymsPutative acyl-CoA dehydrogenase
EC 1.3.99.-
Acyl-CoA dehydrogenase
MCAD
EC 1.3.99.3
MCAD
EC 1.3.99.3

KEGG pathways
MAP codePathways
MAP00071Fatty acid metabolism
MAP00280Valine, leucine and isoleucine degradation
MAP00410beta-Alanine metabolism
MAP00640Propanoate metabolism

Swiss-prot:Accession NumberQ72JJ3Q5SGZ2P41367P11310
Entry nameQ72JJ3_THET2Q5SGZ2_THET8ACADM_PIGACADM_HUMAN
Activity

A medium-chain acyl-CoA + electron-transfer flavoprotein = a medium-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein.A medium-chain acyl-CoA + electron-transfer flavoprotein = a medium-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein.
Subunit

Homotetramer.Homotetramer. Interacts with the heterodimeric electron transfer flavoprotein ETF.
Subcellular location

Mitochondrion matrix.Mitochondrion matrix.
Cofactor

FAD.FAD.


CofactorsSubstratesProducts
KEGG-idC00016C00040C04253C00605C04570
CompoundFADAcyl-CoAElectron-transferring flavoprotein2,3-Dehydroacyl-CoAReduced electron-transferring flavoprotein
Typeamide group,amine group,aromatic ring (only carbon atom),aromatic ring (with nitrogen atoms),carbohydrate,nucleotideamine group,carbohydrate,nucleotide,peptide/protein,sulfide groupamide group,amine group,aromatic ring (only carbon atom),aromatic ring (with nitrogen atoms),carbohydrate,peptide/protein,phosphate group/phosphate ionamine group,carbohydrate,nucleotide,peptide/protein,sulfide groupamide group,amine group,aromatic ring (only carbon atom),aromatic ring (with nitrogen atoms),carbohydrate,peptide/protein,phosphate group/phosphate ion
1ukwA01UnboundUnboundUnboundUnboundUnbound
1ukwB01UnboundUnboundUnboundUnboundUnbound
2cx9A01UnboundUnboundUnboundUnboundUnbound
2cx9B01UnboundUnboundUnboundUnboundUnbound
2cx9C01UnboundUnboundUnboundUnboundUnbound
2cx9D01UnboundUnboundUnboundUnboundUnbound
1udyA01UnboundUnboundUnboundUnboundUnbound
1udyB01UnboundUnboundUnboundUnboundUnbound
1udyC01UnboundUnboundUnboundUnboundUnbound
1udyD01UnboundUnboundUnboundUnboundUnbound
3mddA01UnboundUnboundUnboundUnboundUnbound
3mddB01UnboundUnboundUnboundUnboundUnbound
3mdeA01UnboundUnboundUnboundUnboundUnbound
3mdeB01UnboundUnboundUnboundUnboundUnbound
1egcA01UnboundUnboundUnboundUnboundUnbound
1egcB01UnboundUnboundUnboundUnboundUnbound
1egcC01UnboundUnboundUnboundUnboundUnbound
1egcD01UnboundUnboundUnboundUnboundUnbound
1egdA01UnboundUnboundUnboundUnboundUnbound
1egdB01UnboundUnboundUnboundUnboundUnbound
1egdC01UnboundUnboundUnboundUnboundUnbound
1egdD01UnboundUnboundUnboundUnboundUnbound
1egeA01UnboundUnboundUnboundUnboundUnbound
1egeB01UnboundUnboundUnboundUnboundUnbound
1egeC01UnboundUnboundUnboundUnboundUnbound
1egeD01UnboundUnboundUnboundUnboundUnbound
1t9gA01UnboundUnboundUnboundUnboundUnbound
1t9gB01UnboundUnboundUnboundUnboundUnbound
1t9gC01UnboundUnboundUnboundUnboundUnbound
1t9gD01UnboundUnboundBound:TYR 192-ALA 193-THR 194-LEU 195(chain S)UnboundUnbound
2a1tA01UnboundUnboundUnboundUnboundUnbound
2a1tB01UnboundUnboundUnboundUnboundUnbound
2a1tC01UnboundUnboundUnboundUnboundUnbound
2a1tD01UnboundUnboundBound:TYR 192-ALA 193-THR 194-LEU 195(chain S)UnboundUnbound
1ukwA02Bound:FADUnboundUnboundUnboundUnbound
1ukwB02Bound:FADUnboundUnboundUnboundUnbound
2cx9A02UnboundUnboundUnboundUnboundUnbound
2cx9B02UnboundUnboundUnboundUnboundUnbound
2cx9C02UnboundUnboundUnboundUnboundUnbound
2cx9D02UnboundUnboundUnboundUnboundUnbound
1udyA02Bound:FADUnboundUnboundUnboundUnbound
1udyB02Bound:FADUnboundUnboundUnboundUnbound
1udyC02Bound:FADUnboundUnboundUnboundUnbound
1udyD02Bound:FADUnboundUnboundUnboundUnbound
3mddA02Bound:FADUnboundUnboundUnboundUnbound
3mddB02Bound:FADUnboundUnboundUnboundUnbound
3mdeA02Bound:FADUnboundUnboundUnboundUnbound
3mdeB02Bound:FADUnboundUnboundUnboundUnbound
1egcA02Bound:FADUnboundUnboundUnboundUnbound
1egcB02Bound:FADUnboundUnboundUnboundUnbound
1egcC02Bound:FADUnboundUnboundUnboundUnbound
1egcD02Bound:FADUnboundUnboundUnboundUnbound
1egdA02Bound:FADUnboundUnboundUnboundUnbound
1egdB02Bound:FADUnboundUnboundUnboundUnbound
1egdC02Bound:FADUnboundUnboundUnboundUnbound
1egdD02Bound:FADUnboundUnboundUnboundUnbound
1egeA02Bound:FADUnboundUnboundUnboundUnbound
1egeB02Bound:FADUnboundUnboundUnboundUnbound
1egeC02Bound:FADUnboundUnboundUnboundUnbound
1egeD02Bound:FADUnboundUnboundUnboundUnbound
1t9gA02Bound:FADUnboundUnboundUnboundUnbound
1t9gB02Bound:FADUnboundUnboundUnboundUnbound
1t9gC02Bound:FADUnboundUnboundUnboundUnbound
1t9gD02Bound:FADUnboundUnboundUnboundUnbound
2a1tA02Bound:FADUnboundUnboundUnboundUnbound
2a1tB02Bound:FADUnboundUnboundUnboundUnbound
2a1tC02Bound:FADUnboundBound:FAD(chain R)UnboundUnbound
2a1tD02Bound:FADUnboundUnboundUnboundUnbound
1ukwA03UnboundUnboundUnboundUnboundUnbound
1ukwB03UnboundUnboundUnboundUnboundUnbound
2cx9A03UnboundUnboundUnboundUnboundUnbound
2cx9B03UnboundUnboundUnboundUnboundUnbound
2cx9C03UnboundUnboundUnboundUnboundUnbound
2cx9D03UnboundUnboundUnboundUnboundUnbound
1udyA03UnboundAnalogue:CS8UnboundUnboundUnbound
1udyB03UnboundAnalogue:CS8UnboundUnboundUnbound
1udyC03UnboundAnalogue:CS8UnboundUnboundUnbound
1udyD03UnboundAnalogue:CS8UnboundUnboundUnbound
3mddA03UnboundUnboundUnboundUnboundUnbound
3mddB03UnboundUnboundUnboundUnboundUnbound
3mdeA03UnboundBound:CO8UnboundUnboundUnbound
3mdeB03UnboundBound:CO8UnboundUnboundUnbound
1egcA03UnboundBound:CO8UnboundUnboundUnbound
1egcB03UnboundBound:CO8UnboundUnboundUnbound
1egcC03UnboundBound:CO8UnboundUnboundUnbound
1egcD03UnboundBound:CO8UnboundUnboundUnbound
1egdA03UnboundUnboundUnboundUnboundUnbound
1egdB03UnboundUnboundUnboundUnboundUnbound
1egdC03UnboundUnboundUnboundUnboundUnbound
1egdD03UnboundUnboundUnboundUnboundUnbound
1egeA03UnboundUnboundUnboundUnboundUnbound
1egeB03UnboundUnboundUnboundUnboundUnbound
1egeC03UnboundUnboundUnboundUnboundUnbound
1egeD03UnboundUnboundUnboundUnboundUnbound
1t9gA03UnboundUnboundUnboundUnboundUnbound
1t9gB03UnboundUnboundUnboundUnboundUnbound
1t9gC03UnboundUnboundUnboundUnboundUnbound
1t9gD03UnboundUnboundUnboundUnboundUnbound
2a1tA03UnboundUnboundUnboundUnboundUnbound
2a1tB03UnboundUnboundUnboundUnboundUnbound
2a1tC03UnboundUnboundUnboundUnboundUnbound
2a1tD03UnboundUnboundUnboundUnboundUnbound

Active-site residues
resource
PDB;1egc, 1egd, 1ege, 3mde & Swiss-prot;P11310, P41367 & literature [6], [15], [21], [24], [32], [35], [39], [54]
pdbCatalytic residuesMain-chain involved in catalysiscomment
1ukwA01       


1ukwB01       


2cx9A01       


2cx9B01       


2cx9C01       


2cx9D01       


1udyA01       


1udyB01       


1udyC01       


1udyD01       


3mddA01       


3mddB01       


3mdeA01       


3mdeB01       


1egcA01       


1egcB01       


1egcC01       


1egcD01       


1egdA01       


1egdB01       


1egdC01       


1egdD01       


1egeA01       


1egeB01       


1egeC01       


1egeD01       


1t9gA01       


1t9gB01       


1t9gC01       


1t9gD01       


2a1tA01       


2a1tB01       


2a1tC01       


2a1tD01       


1ukwA02       


1ukwB02       


2cx9A02       


2cx9B02       


2cx9C02       


2cx9D02       


1udyA02       


1udyB02       


1udyC02       


1udyD02       


3mddA02       


3mddB02       


3mdeA02       


3mdeB02       


1egcA02       


1egcB02       


1egcC02       


1egcD02       


1egdA02       


1egdB02       


1egdC02       


1egdD02       


1egeA02       


1egeB02       


1egeC02       


1egeD02       


1t9gA02       


1t9gB02       


1t9gC02       


1t9gD02       


2a1tA02       


2a1tB02       


2a1tC02       


2a1tD02       


1ukwA03GLU 393
GLU 393

1ukwB03GLU 393
GLU 393

2cx9A03GLU 369
GLU 369

2cx9B03GLU 369
GLU 369

2cx9C03GLU 369
GLU 369

2cx9D03GLU 369
GLU 369

1udyA03GLU 376
GLU 376

1udyB03GLU 376
GLU 376

1udyC03GLU 376
GLU 376

1udyD03GLU 376
GLU 376

3mddA03GLU 376
GLU 376

3mddB03GLU 376
GLU 376

3mdeA03GLU 376
GLU 376

3mdeB03GLU 376
GLU 376

1egcA03       

mutant T255E, E376G
1egcB03       

mutant T255E, E376G
1egcC03       

mutant T255E, E376G
1egcD03       

mutant T255E, E376G
1egdA03       

mutant T255E, E376G
1egdB03       

mutant T255E, E376G
1egdC03       

mutant T255E, E376G
1egdD03       

mutant T255E, E376G
1egeA03GLU 376
GLU 376
mutant T255E
1egeB03GLU 376
GLU 376
mutant T255E
1egeC03GLU 376
GLU 376
mutant T255E
1egeD03GLU 376
GLU 376
mutant T255E
1t9gA03GLU 376
GLU 376

1t9gB03GLU 376
GLU 376

1t9gC03GLU 376
GLU 376

1t9gD03GLU 376
GLU 376

2a1tA03GLU 376
GLU 376

2a1tB03GLU 376
GLU 376

2a1tC03GLU 376
GLU 376

2a1tD03GLU 376
GLU 376


References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[1]Scheme 2
[4]p.417
[15]p.7525-7527
[19]Scheme 1
[21]Scheme 3, p.719, p.722-723
[22]Fig.10, Fig.11, p.805-807
[24]p.12417-12420
[30]Scheme 1
[31]Fig.4, p.14609-14612
[32]p.1701-1704
[35]Scheme 1, Scheme 2, Scheme 5, p.8443-8444
[36]p.8454
[37]Scheme 1, p.1856-1860
[38]Fig.1, Fig.3
[39]Fig.1, p.226
[40]Scheme 4, p.264-266
[41]Scheme 1, Fig.7
[42]Scheme 2, p.13989-13991
[45]Scheme 1
[50]Scheme 1, p.4638
[50]Fig.8, p.4645-4647
[53]Scheme 1, Scheme 2, p.11852-11855
[54]p.301-303
[55]p.488-491
[56]

[58]Fig.5

references
[1]
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Year1985
Volume260
Pages1326-37
AuthorsIkeda Y, Hine DG, Okamura-Ikeda K, Tanaka K
TitleMechanism of action of short-chain, medium-chain, and long-chain acyl-CoA dehydrogenases. Direct evidence for carbanion formation as an intermediate step using enzyme-catalyzed C-2 proton/deuteron exchange in the absence of C-3 exchange.
[2]
PubMed ID3769916
JournalEur J Biochem
Year1986
Volume160
Pages109-15
AuthorsPohl B, Raichle T, Ghisla S
TitleStudies on the reaction mechanism of general acyl-CoA dehydrogenase. Determination of selective isotope effects in the dehydrogenation of butyryl-CoA.
[3]
PubMed ID3115254
JournalBiochem J
Year1987
Volume243
Pages519-24
AuthorsSteenkamp DJ
TitlePreferential cross-linking of the small subunit of the electron-transfer flavoprotein to general acyl-CoA dehydrogenase.
[4]
PubMed ID3053288
JournalBiochem Soc Trans
Year1988
Volume16
Pages416-8
AuthorsFrerman FE
TitleAcyl-CoA dehydrogenases, electron transfer flavoprotein and electron transfer flavoprotein dehydrogenase.
[5]
PubMed ID3413116
JournalProc Natl Acad Sci U S A
Year1988
Volume85
Pages6677-81
AuthorsKim JJ, Wu J
TitleStructure of the medium-chain acyl-CoA dehydrogenase from pig liver mitochondria at 3-A resolution.
[6]
PubMed ID1970566
JournalJ Biol Chem
Year1990
Volume265
Pages7116-9
AuthorsBross P, Engst S, Strauss AW, Kelly DP, Rasched I, Ghisla S
TitleCharacterization of wild-type and an active site mutant of human medium chain acyl-CoA dehydrogenase after expression in Escherichia coli.
[7]
CommentsVARIANT MCAD GLU-329.
Medline ID91067682
PubMed ID2251268
JournalProc Natl Acad Sci U S A
Year1990
Volume87
Pages9236-40
AuthorsKelly DP, Whelan AJ, Ogden ML, Alpers R, Zhang ZF, Bellus G, Gregersen N, Dorland L, Strauss AW
TitleMolecular characterization of inherited medium-chain acyl-CoA dehydrogenase deficiency.
Related Swiss-protP11310
[8]
PubMed ID2326312
JournalProg Clin Biol Res
Year1990
Volume321
Pages569-76
AuthorsKim JJ, Wu J
TitleStructural studies of medium-chain acyl-CoA dehydrogenase from pig liver mitochondria.
[9]
CommentsT00007-5
PubMed ID1931995
JournalBiochemistry
Year1991
Volume30
Pages10755-60
AuthorsTserng KY, Jin SJ, Hoppel CL
TitleSpiropentaneacetic acid as a specific inhibitor of medium-chain acyl-CoA dehydrogenase.
[10]
CommentsVARIANT MCAD GLU-329.
Medline ID91224627
PubMed ID1902818
JournalHum Genet
Year1991
Volume86
Pages545-51
AuthorsGregersen N, Andresen BS, Bross P, Winter V, Rudiger N, Engst S, Christensen E, Kelly D, Strauss AW, Kolvraa S, et al
TitleMolecular characterization of medium-chain acyl-CoA dehydrogenase (MCAD) deficiency: identification of a lys329 to glu mutation in the MCAD gene, and expression of inactive mutant enzyme protein in E. coli.
Related Swiss-protP11310
[11]
CommentsT00007-6
PubMed ID8102510
JournalAm J Hum Genet
Year1993
Volume53
Pages730-9
AuthorsAndresen BS, Bross P, Jensen TG, Winter V, Knudsen I, Kolvraa S, Jensen UB, Bolund L, Duran M, Kim JJ, et al
TitleA rare disease-associated mutation in the medium-chain acyl-CoA dehydrogenase (MCAD) gene changes a conserved arginine, previously shown to be functionally essential in short-chain acyl-CoA dehydrogenase (SCAD).
[12]
PubMed ID8218225
JournalBiochemistry
Year1993
Volume32
Pages11575-85
AuthorsJohnson JK, Kumar NR, Srivastava DK
TitleMicroscopic pathway for the medium-chain fatty acyl CoA dehydrogenase catalyzed oxidative half-reaction: changes in the electronic structures of flavin and CoA derivatives during catalysis.
[13]
PubMed ID8267794
JournalBiochemistry
Year1993
Volume32
Pages8004-13
AuthorsJohnson JK, Srivastava DK
TitleDetection and identification of a chromophoric intermediate during the medium-chain fatty acyl-CoA dehydrogenase-catalyzed reaction via rapid-scanning UV/visible spectroscopy.
[14]
PubMed ID8454567
JournalJ Biochem (Tokyo)
Year1993
Volume113
Pages106-13
AuthorsMiura R, Nishina Y, Sato K, Fujii S, Kuroda K, Shiga K
Title13C- and 15N-NMR studies on medium-chain acyl-CoA dehydrogenase reconstituted with 13C- and 15N-enriched flavin adenine dinucleotide.
[15]
CommentsX-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
Medline ID93361479
PubMed ID8356049
JournalProc Natl Acad Sci U S A
Year1993
Volume90
Pages7523-7
AuthorsKim JJ, Wang M, Paschke R
TitleCrystal structures of medium-chain acyl-CoA dehydrogenase from pig liver mitochondria with and without substrate.
Related PDB3mdd,3mde
Related Swiss-protP41367
[16]
PubMed ID8161532
JournalBiochemistry
Year1994
Volume33
Pages4738-44
AuthorsJohnson JK, Kumar NR, Srivastava DK
TitleMolecular basis of the medium-chain fatty acyl-CoA dehydrogenase-catalyzed "oxidase" reaction: pH-dependent distribution of intermediary enzyme species during catalysis.
[17]
PubMed ID7905878
JournalJ Biol Chem
Year1994
Volume269
Pages4401-8
AuthorsSaijo T, Welch WJ, Tanaka K
TitleIntramitochondrial folding and assembly of medium-chain acyl-CoA dehydrogenase (MCAD). Demonstration of impaired transfer of K304E-variant MCAD from its complex with hsp60 to the native tetramer.
[18]
PubMed ID7703241
JournalBiochemistry
Year1995
Volume34
Pages4276-86
AuthorsFitzsimmons ME, Thorpe C, Anders MW
TitleMedium-chain acyl-CoA dehydrogenase- and enoyl-CoA hydratase-dependent bioactivation of 5,6-dichloro-4-thia-5-hexenoyl-CoA.
[19]
PubMed ID8845370
JournalBiochemistry
Year1995
Volume34
Pages16424-32
AuthorsSchaller RA, Thorpe C
TitleOxidative inactivation of a charge transfer complex in the medium-chain acyl-CoA dehydrogenase.
[20]
PubMed ID7718565
JournalBiochemistry
Year1995
Volume34
Pages4625-32
AuthorsSrivastava DK, Kumar NR, Peterson KL
Title"Dehydrogenase" and "oxidase" reactions of medium-chain fatty acyl-CoA dehydrogenase utilizing chromogenic substrates: role of the 3',5'-adenosine diphosphate moiety of the coenzyme A thioester in catalysis.
[21]
PubMed ID7601336
JournalFASEB J
Year1995
Volume9
Pages718-25
AuthorsThorpe C, Kim JJ
TitleStructure and mechanism of action of the acyl-CoA dehydrogenases.
[22]
PubMed ID7592542
JournalJ Biochem (Tokyo)
Year1995
Volume117
Pages800-8
AuthorsNishina Y, Sato K, Hazekawa I, Shiga K
TitleStructural modulation of 2-enoyl-CoA bound to reduced acyl-CoA dehydrogenases: a resonance Raman study of a catalytic intermediate.
[23]
PubMed ID7730333
JournalJ Biol Chem
Year1995
Volume270
Pages10284-90
AuthorsBross P, Jespersen C, Jensen TG, Andresen BS, Kristensen MJ, Winter V, Nandy A, Krautle F, Ghisla S, Bolundi L, et al
TitleEffects of two mutations detected in medium chain acyl-CoA dehydrogenase (MCAD)-deficient patients on folding, oligomer assembly, and stability of MCAD enzyme.
[24]
CommentsX-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
Medline ID96420477
PubMed ID8823176
JournalBiochemistry
Year1996
Volume35
Pages12412-20
AuthorsLee HJ, Wang M, Paschke R, Nandy A, Ghisla S, Kim JJ
TitleCrystal structures of the wild type and the Glu376Gly/Thr255Glu mutant of human medium-chain acyl-CoA dehydrogenase: influence of the location of the catalytic base on substrate specificity.
Related PDB1egc,1egd,1ege
Related Swiss-protP11310
[25]
PubMed ID8823175
JournalBiochemistry
Year1996
Volume35
Pages12402-11
AuthorsNandy A, Kieweg V, Krautle FG, Vock P, Kuchler B, Bross P, Kim JJ, Rasched I, Ghisla S
TitleMedium-long-chain chimeric human Acyl-CoA dehydrogenase: medium-chain enzyme with the active center base arrangement of long-chain Acyl-CoA dehydrogenase.
[26]
PubMed ID9271097
JournalBiochem J
Year1997
Volume325
Pages751-60
AuthorsPeterson KL, Srivastava DK
TitleFunctional role of a distal (3'-phosphate) group of CoA in the recombinant human liver medium-chain acyl-CoA dehydrogenase-catalysed reaction.
[27]
PubMed ID9426198
JournalBiol Chem
Year1997
Volume378
Pages1381-5
AuthorsMacheroux P, Sanner C, Buttner H, Kieweg V, Ruterjans H, Ghisla S
TitleMedium-chain acyl CoA dehydrogenase: evidence for phosphorylation.
[28]
PubMed ID9434899
JournalCurr Opin Struct Biol
Year1997
Volume7
Pages804-10
AuthorsMattevi A, Vanoni MA, Curti B
TitleStructure of D-amino acid oxidase: new insights from an old enzyme.
[29]
PubMed ID9208949
JournalEur J Biochem
Year1997
Volume246
Pages548-56
AuthorsKieweg V, Krautle FG, Nandy A, Engst S, Vock P, Abdel-Ghany AG, Bross P, Gregersen N, Rasched I, Strauss A, Ghisla S
TitleBiochemical characterization of purified, human recombinant Lys304-->Glu medium-chain acyl-CoA dehydrogenase containing the common disease-causing mutation and comparison with the normal enzyme.
[30]
PubMed ID9477967
JournalBiochemistry
Year1998
Volume37
Pages1383-93
AuthorsBaker-Malcolm JF, Haeffner-Gormley L, Wang L, Anders MW, Thorpe C
TitleElimination reactions in the medium-chain acyl-CoA dehydrogenase: bioactivation of cytotoxic 4-thiaalkanoic acids.
[31]
PubMed ID9772189
JournalBiochemistry
Year1998
Volume37
Pages14605-12
AuthorsMancini-Samuelson GJ, Kieweg V, Sabaj KM, Ghisla S, Stankovich MT
TitleRedox properties of human medium-chain acyl-CoA dehydrogenase, modulation by charged active-site amino acid residues.
[32]
PubMed ID9484241
JournalBiochemistry
Year1998
Volume37
Pages1697-705
AuthorsPeterson KL, Galitz DS, Srivastava DK
TitleInfluence of excision of a methylene group from Glu-376 (Glu376-->Asp mutation) in the medium chain acyl-CoA dehydrogenase-catalyzed reaction.
[33]
PubMed ID9730839
JournalBiochemistry
Year1998
Volume37
Pages12659-71
AuthorsPeterson KL, Peterson KM, Srivastava DK
TitleThermodynamics of ligand binding and catalysis in human liver medium-chain acyl-CoA dehydrogenase: comparative studies involving normal and 3'-dephosphorylated C8-CoAs and wild-type and Asn191 --> Ala (N191A) mutant enzymes.
[34]
PubMed ID9521671
JournalBiochemistry
Year1998
Volume37
Pages3499-508
AuthorsQin L, Srivastava DK
TitleEnergetics of two-step binding of a chromophoric reaction product, trans-3-indoleacryloyl-CoA, to medium-chain acyl-coenzyme-A dehydrogenase.
[35]
PubMed ID9622495
JournalBiochemistry
Year1998
Volume37
Pages8437-45
AuthorsRudik I, Ghisla S, Thorpe C
TitleProtonic equilibria in the reductive half-reaction of the medium-chain acyl-CoA dehydrogenase.
[36]
PubMed ID9622496
JournalBiochemistry
Year1998
Volume37
Pages8446-56
AuthorsSrivastava DK, Peterson KL
TitleDiscriminatory influence of Glu-376-->Asp mutation in medium-chain acyl-CoA dehydrogenase on the binding of selected CoA-ligands: spectroscopic, thermodynamic, kinetic, and model building studies.
[37]
PubMed ID9485310
JournalBiochemistry
Year1998
Volume37
Pages1848-60
AuthorsVock P, Engst S, Eder M, Ghisla S
TitleSubstrate activation by acyl-CoA dehydrogenases: transition-state stabilization and pKs of involved functional groups.
[38]
PubMed ID10496972
JournalArch Biochem Biophys
Year1999
Volume370
Pages16-21
AuthorsStankovich MT, Sabaj KM, Tonge PJ
TitleStructure/function of medium chain acyl-CoA dehydrogenase: the importance of substrate polarization.
[39]
PubMed ID9882619
JournalBiochem J
Year1999
Volume337
Pages225-30
AuthorsKuchler B, Abdel-Ghany AG, Bross P, Nandy A, Rasched I, Ghisla S
TitleBiochemical characterization of a variant human medium-chain acyl-CoA dehydrogenase with a disease-associated mutation localized in the active site.
[40]
PubMed ID9890906
JournalBiochemistry
Year1999
Volume38
Pages257-67
AuthorsEngst S, Vock P, Wang M, Kim JJ, Ghisla S
TitleMechanism of activation of acyl-CoA substrates by medium chain acyl-CoA dehydrogenase: interaction of the thioester carbonyl with the flavin adenine dinucleotide ribityl side chain.
[41]
PubMed ID9990125
JournalJ Biochem (Tokyo)
Year1999
Volume125
Pages285-96
AuthorsTamaoki H, Nishina Y, Shiga K, Miura R
TitleMechanism for the recognition and activation of substrate in medium-chain acyl-CoA dehydrogenase.
[42]
PubMed ID11076541
JournalBiochemistry
Year2000
Volume39
Pages13982-92
AuthorsPellett JD, Sabaj KM, Stephens AW, Bell AF, Wu J, Tonge PJ, Stankovich MT
TitleMedium-chain acyl-coenzyme A dehydrogenase bound to a product analogue, hexadienoyl-coenzyme A: effects on reduction potential, pK(a), and polarization.
[43]
PubMed ID11027146
JournalBiochemistry
Year2000
Volume39
Pages12659-70
AuthorsPeterson KM, Gopalan KV, Srivastava DK
TitleInfluence of alpha-CH-->NH substitution in C8-CoA on the kinetics of association and dissociation of ligands with medium chain acyl-CoA dehydrogenase.
[44]
PubMed ID11027148
JournalBiochemistry
Year2000
Volume39
Pages12678-87
AuthorsPeterson KM, Srivastava DK
TitleEnergetic consequences of accommodating a bulkier ligand at the active site of medium chain acyl-CoA dehydrogenase by creating a complementary enzyme site cavity.
[45]
PubMed ID10625483
JournalBiochemistry
Year2000
Volume39
Pages92-101
AuthorsRudik I, Bell A, Tonge PJ, Thorpe C
Title4-Hydroxycinnamoyl-CoA: an ionizable probe of the active site of the medium chain acyl-CoA dehydrogenase.
[46]
PubMed ID10694883
JournalTrends Biochem Sci
Year2000
Volume25
Pages126-32
AuthorsFraaije MW, Mattevi A
TitleFlavoenzymes: diverse catalysts with recurrent features.
[47]
PubMed ID11488611
JournalArch Biochem Biophys
Year2001
Volume392
Pages341-8
AuthorsRudik I, Thorpe C
TitleThioester enolate stabilization in the acyl-CoA dehydrogenases: the effect of 5-deaza-flavin substitution.
[48]
PubMed ID11591145
JournalBiochemistry
Year2001
Volume40
Pages12266-75
AuthorsWang W, Fu Z, Zhou JZ, Kim JJ, Thorpe C
TitleInteraction of 3,4-dienoyl-CoA thioesters with medium chain acyl-CoA dehydrogenase: stereochemistry of inactivation of a flavoenzyme.
[49]
CommentsVARIANT MCAD LEU-245.
Medline ID21302532
PubMed ID11409868
JournalHum Genet
Year2001
Volume108
Pages404-8
AuthorsZschocke J, Schulze A, Lindner M, Fiesel S, Olgemoller K, Hoffmann GF, Penzien J, Ruiter JP, Wanders RJ, Mayatepek E
TitleMolecular and functional characterisation of mild MCAD deficiency.
Related Swiss-protP11310
[50]
PubMed ID11926826
JournalBiochemistry
Year2002
Volume41
Pages4638-48
AuthorsGopalan KV, Srivastava DK
TitleBeyond the proton abstracting role of Glu-376 in medium-chain acyl-CoA dehydrogenase: influence of Glu-376-->Gln substitution on ligand binding and catalysis.
[51]
PubMed ID11872165
JournalJ Biochem (Tokyo)
Year2002
Volume131
Pages365-74
AuthorsNakajima Y, Miyahara I, Hirotsu K, Nishina Y, Shiga K, Setoyama C, Tamaoki H, Miura R
TitleThree-dimensional structure of the flavoenzyme acyl-CoA oxidase-II from rat liver, the peroxisomal counterpart of mitochondrial acyl-CoA dehydrogenase.
[52]
PubMed ID12504892
JournalArch Biochem Biophys
Year2003
Volume409
Pages251-61
AuthorsLamm TR, Kohls TD, Saenger AK, Stankovich MT
TitleComparison of ligand polarization and enzyme activation in medium- and short-chain acyl-coenzyme A dehydrogenase-novel analog complexes.
[53]
PubMed ID14529297
JournalBiochemistry
Year2003
Volume42
Pages11846-56
AuthorsWu J, Bell AF, Luo L, Stephens AW, Stankovich MT, Tonge PJ
TitleProbing hydrogen-bonding interactions in the active site of medium-chain acyl-CoA dehydrogenase using Raman spectroscopy.
[54]
CommentsX|ray crystallography
PubMed ID12966080
JournalJ Biochem (Tokyo)
Year2003
Volume134
Pages297-304
AuthorsSatoh A, Nakajima Y, Miyahara I, Hirotsu K, Tanaka T, Nishina Y, Shiga K, Tamaoki H, Setoyama C, Miura R
TitleStructure of the transition state analog of medium-chain acyl-CoA dehydrogenase. Crystallographic and molecular orbital studies on the charge-transfer complex of medium-chain acyl-CoA dehydrogenase with 3-thiaoctanoyl-CoA.
Related PDB1udy
[55]
PubMed ID14728675
JournalEur J Biochem
Year2004
Volume271
Pages483-93
AuthorsKim JJ, Miura R
TitleAcyl-CoA dehydrogenases and acyl-CoA oxidases. Structural basis for mechanistic similarities and differences.
[56]
CommentsX|ray crystallography
PubMed ID15159392
JournalJ Biol Chem
Year2004
Volume279
Pages32904-12
AuthorsToogood HS, van Thiel A, Basran J, Sutcliffe MJ, Scrutton NS, Leys D
TitleExtensive domain motion and electron transfer in the human electron transferring flavoprotein.medium chain Acyl-CoA dehydrogenase complex.
Related PDB1t9g
[57]
PubMed ID15358373
JournalProtein Expr Purif
Year2004
Volume37
Pages472-8
AuthorsZeng J, Li D
TitleExpression and purification of His-tagged rat mitochondrial medium-chain acyl-CoA dehydrogenase wild-type and Arg256 mutant proteins.
[58]
PubMed ID15975918
JournalJ Biol Chem
Year2005
Volume280
Pages30361-6
AuthorsToogood HS, van Thiel A, Scrutton NS, Leys D
TitleStabilization of non-productive conformations underpins rapid electron transfer to electron-transferring flavoprotein.
Related PDB2a1t

comments
This enzyme is a member of medium-chain acyl-CoA dehydrogenases.
Accoriding to the literature, this enzyme catalyzes the following reactions:
(A) Hydride transfer from acyl-CoA substrate to FAD, giving 2,3-dehydroacyl-CoA and FADH2(Two-electron-reduced form of FAD) (Reductive half-reaction):
(B) Hydride transfer from FADH2 to FAD of an acceptor protein, Electron-Transferring Flavoprotein (ETF):
The ETF protein is heterodimer (alpha/beta subunits) containing one FAD and one AMP per dimer (see [58], Swissprot;P13804, P38117). This protein seems to accept electrons from various oxidoreductases.

createdupdated
2005-05-122012-10-02
Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2010)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)

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